Lodoacetates

The surest way to inhibit an enzyme is to block the active site irreversibly by chemical reaction with some active species to form a covalent bond. Thus, iodoacetate will irreversibly inactivate thiol proteases by forming the stable carboxymethyl mercaptan. lodoacetate is of course non-selective (many other enzymes would be inactivated), toxic (many sensitive sites would be alkylated) and moreover the drug itself is unstable due to its very reactivity. 

Coupling via lodoacetate-Modified Phosphatidylethanolamine Lipid Derivatives... 

Hpall is a restriction endonuclease Helix-tum-helix High-throughput screening Haplotype single-nucleotide polymorphism Human genome organization Human umbilical vein endothelial cells lodoacetic acid... 

Carboxymethylation 50 pL of 10 mM iodoacetamide (made up fresh in 100 mM ammonium bicarbonate in 10% acetonitrile) is added and the tube incubated for 30 min at room temperature in the dark. The supernatant is removed and the gels washed as follows. This step is performed to carboxymethylate the cysteine residues to ensure that disulfide bonds cannot re-form. This increases the molecular weight of the residue by approx 57 Da and needs to be taken into account when the database search is performed (4). lodoacetic acid can be employed, rather than iodoacetamide, but this causes an increase of approx 58 Da in the weight of cysteine residues. 

SYNS lA lODOACETATE MIA MONO-lODOACETATE MONOIODOACETIC ACID... 

SYNS lODOACETATE SODIUM SALT lODOACETIC ACID SODIUM SALT USAF EK-6279... 

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